Biochemical Characterization of Apoptotic Cleavage of KH-Type Splicing Regulatory Protein (KSRP) / Far Upstream Element-Binding Protein 2 (FBP2)
| Autor: | Minseok Cheon, II-Seon Park, Heeyoung Seok, Jinsun Cho |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Regulation of gene expression
biology Caspase 3 Intrinsic apoptosis RNA-Binding Proteins Apoptosis General Medicine Cleavage (embryo) Biochemistry Cysteine protease Rats Substrate Specificity Structural Biology Caspases RNA splicing Proteome Trans-Activators Tumor Cells Cultured biology.protein Animals Humans Caspase |
| Zdroj: | Protein & Peptide Letters. 9:511-519 |
| ISSN: | 0929-8665 |
| DOI: | 10.2174/0929866023408454 |
| Popis: | Caspases, Asp-specific cysteine protease, cleave proteins upon apoptosis. To identify and characterize new caspase substrate in the nucleus, the proteome of the rat liver extracts was analyzed after the treatment with caspases. One of the identified proteins was KSRP / FBP2 that is preferentially cleaved by caspase-3 and -7 at two sites after Asp102 and Asp183. The second site was cleaved only in the protein produced in cells, but not in in vitro translated protein. These results indicate that more than the primary sequence may be important for the recognition by caspases. |
| Databáze: | OpenAIRE |
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